BP08_BPT4
ID BP08_BPT4 Reviewed; 334 AA.
AC P19062;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 29-SEP-2021, entry version 104.
DE RecName: Full=Baseplate wedge protein gp8 {ECO:0000305};
DE AltName: Full=Gene product 8;
DE Short=gp8;
GN Name=8;
OS Enterobacteria phage T4 (Bacteriophage T4).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Myoviridae; Tevenvirinae; Tequatrovirus.
OX NCBI_TaxID=10665;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=D;
RX PubMed=2402473; DOI=10.1093/nar/18.17.5313;
RA Efimov V.P., Prilipov A.G., Mesyanzhinov V.V.;
RT "Nucleotide sequences of bacteriophage T4 genes 6, 7 and 8.";
RL Nucleic Acids Res. 18:5313-5313(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12626685; DOI=10.1128/mmbr.67.1.86-156.2003;
RA Miller E.S., Kutter E., Mosig G., Arisaka F., Kunisawa T., Ruger W.;
RT "Bacteriophage T4 genome.";
RL Microbiol. Mol. Biol. Rev. 67:86-156(2003).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=2403438; DOI=10.1128/jvi.64.1.143-154.1990;
RA Watts N.R., Coombs D.H.;
RT "Structure of the bacteriophage T4 baseplate as determined by chemical
RT cross-linking.";
RL J. Virol. 64:143-154(1990).
RN [4]
RP REVIEW.
RX PubMed=14625682; DOI=10.1007/s00018-003-3072-1;
RA Leiman P.G., Kanamaru S., Mesyanzhinov V.V., Arisaka F., Rossmann M.G.;
RT "Structure and morphogenesis of bacteriophage T4.";
RL Cell. Mol. Life Sci. 60:2356-2370(2003).
RN [5]
RP REVIEW ON FUNCTION.
RX PubMed=21129200; DOI=10.1186/1743-422x-7-355;
RA Leiman P.G., Arisaka F., van Raaij M.J., Kostyuchenko V.A., Aksyuk A.A.,
RA Kanamaru S., Rossmann M.G.;
RT "Morphogenesis of the T4 tail and tail fibers.";
RL Virol. J. 7:355-355(2010).
RN [6]
RP SUBUNIT.
RX PubMed=19896486; DOI=10.1016/j.jmb.2009.10.071;
RA Yap M.L., Mio K., Leiman P.G., Kanamaru S., Arisaka F.;
RT "The baseplate wedges of bacteriophage T4 spontaneously assemble into
RT hubless baseplate-like structure in vitro.";
RL J. Mol. Biol. 395:349-360(2010).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 7-334.
RX PubMed=12729757; DOI=10.1016/s0022-2836(03)00366-8;
RA Leiman P.G., Shneider M.M., Kostyuchenko V.A., Chipman P.R.,
RA Mesyanzhinov V.V., Rossmann M.G.;
RT "Structure and location of gene product 8 in the bacteriophage T4
RT baseplate.";
RL J. Mol. Biol. 328:821-833(2003).
RN [8]
RP STRUCTURE BY ELECTRON MICROSCOPY (17.0 ANGSTROMS) OF THE CONTRACTED TAIL,
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=15315755; DOI=10.1016/j.cell.2004.07.022;
RA Leiman P.G., Chipman P.R., Kostyuchenko V.A., Mesyanzhinov V.V.,
RA Rossmann M.G.;
RT "Three-dimensional rearrangement of proteins in the tail of bacteriophage
RT T4 on infection of its host.";
RL Cell 118:419-429(2004).
RN [9]
RP STRUCTURE BY ELECTRON MICROSCOPY (4.11 ANGSTROMS), SUBUNIT, SUBCELLULAR
RP LOCATION, AND FUNCTION.
RX PubMed=27193680; DOI=10.1038/nature17971;
RA Taylor N.M., Prokhorov N.S., Guerrero-Ferreira R.C., Shneider M.M.,
RA Browning C., Goldie K.N., Stahlberg H., Leiman P.G.;
RT "Structure of the T4 baseplate and its function in triggering sheath
RT contraction.";
RL Nature 533:346-352(2016).
CC -!- FUNCTION: Intermediate baseplate protein. Involved in the tail
CC assembly. {ECO:0000269|PubMed:15315755, ECO:0000269|PubMed:27193680,
CC ECO:0000303|PubMed:21129200}.
CC -!- SUBUNIT: Homodimer (PubMed:2403438, PubMed:19896486, PubMed:27193680).
CC Interacts with gp7. Part of the baseplate macromolecular complex which
CC consists of gp5, gp5.4, gp27 (central spike complex); gp6, gp25, gp53
CC (inner baseplate); gp7, gp8 (intermediate baseplate); gp9, gp10, gp11,
CC gp12 (peripheral); gp48 and gp54 (proximal region of the tail tube).
CC {ECO:0000269|PubMed:19896486, ECO:0000269|PubMed:27193680}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:2403438,
CC ECO:0000269|PubMed:27193680}. Note=Present in 12 copies in the
CC baseplate. {ECO:0000303|PubMed:21129200}.
CC -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the tevenvirinae baseplate structural protein
CC gp8 family. {ECO:0000305}.
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DR EMBL; X15907; CAA34023.1; -; Genomic_DNA.
DR EMBL; AF158101; AAD42519.1; -; Genomic_DNA.
DR PIR; JQ0658; G8BPT4.
DR RefSeq; NP_049766.1; NC_000866.4.
DR PDB; 1N7Z; X-ray; 2.00 A; A/B/C/D=1-334.
DR PDB; 1N80; X-ray; 2.45 A; A/B/C/D=1-334.
DR PDB; 1N8B; X-ray; 2.90 A; A/B/C/D=1-334.
DR PDB; 1PDM; EM; 12.00 A; A/B/C/D/E/F/G/H/I/J/K/L=1-334.
DR PDB; 1TJA; EM; 16.00 A; A/B=1-334.
DR PDB; 5HX2; EM; 3.80 A; B/C=1-334.
DR PDB; 5IV5; EM; 4.11 A; CA/CB/D/E/ED/EE/GG/GH/a/b/x/y=1-334.
DR PDB; 5IV7; EM; 6.77 A; AA/CB/CC/D/E/ED/EE/T/U/j/k/z=1-334.
DR PDBsum; 1N7Z; -.
DR PDBsum; 1N80; -.
DR PDBsum; 1N8B; -.
DR PDBsum; 1PDM; -.
DR PDBsum; 1TJA; -.
DR PDBsum; 5HX2; -.
DR PDBsum; 5IV5; -.
DR PDBsum; 5IV7; -.
DR SMR; P19062; -.
DR TCDB; 1.K.1.1.1; the gp27/5 t4-baseplate (t4-bp) family.
DR GeneID; 1258542; -.
DR KEGG; vg:1258542; -.
DR EvolutionaryTrace; P19062; -.
DR Proteomes; UP000009087; Genome.
DR GO; GO:0098025; C:virus tail, baseplate; IDA:UniProtKB.
DR GO; GO:0098003; P:viral tail assembly; IEA:UniProtKB-KW.
DR InterPro; IPR036327; Gp8_sf.
DR InterPro; IPR015298; Phage_T4_Gp8.
DR Pfam; PF09215; Phage-Gp8; 1.
DR SUPFAM; SSF89433; SSF89433; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Reference proteome; Viral baseplate protein;
KW Viral release from host cell; Viral tail assembly; Viral tail protein;
KW Virion.
FT CHAIN 1..334
FT /note="Baseplate wedge protein gp8"
FT /id="PRO_0000164998"
FT DISULFID 142..153
FT STRAND 9..12
FT /evidence="ECO:0007829|PDB:1N7Z"
FT HELIX 14..27
FT /evidence="ECO:0007829|PDB:1N7Z"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:1N7Z"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:1N7Z"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:1N7Z"
FT HELIX 65..74
FT /evidence="ECO:0007829|PDB:1N7Z"
FT STRAND 75..81
FT /evidence="ECO:0007829|PDB:1N7Z"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:1N7Z"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:1N7Z"
FT STRAND 111..117
FT /evidence="ECO:0007829|PDB:1N7Z"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:1N7Z"
FT STRAND 128..135
FT /evidence="ECO:0007829|PDB:1N7Z"
FT STRAND 138..144
FT /evidence="ECO:0007829|PDB:1N7Z"
FT HELIX 150..155
FT /evidence="ECO:0007829|PDB:1N7Z"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:1N7Z"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:1N8B"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:1N7Z"
FT STRAND 187..194
FT /evidence="ECO:0007829|PDB:1N7Z"
FT HELIX 196..202
FT /evidence="ECO:0007829|PDB:1N7Z"
FT STRAND 205..210
FT /evidence="ECO:0007829|PDB:1N7Z"
FT HELIX 213..218
FT /evidence="ECO:0007829|PDB:1N7Z"
FT HELIX 220..223
FT /evidence="ECO:0007829|PDB:1N7Z"
FT HELIX 231..234
FT /evidence="ECO:0007829|PDB:1N7Z"
FT HELIX 238..241
FT /evidence="ECO:0007829|PDB:1N7Z"
FT STRAND 246..249
FT /evidence="ECO:0007829|PDB:1N7Z"
FT STRAND 251..254
FT /evidence="ECO:0007829|PDB:1N7Z"
FT TURN 255..257
FT /evidence="ECO:0007829|PDB:1N7Z"
FT HELIX 259..262
FT /evidence="ECO:0007829|PDB:1N7Z"
FT STRAND 269..277
FT /evidence="ECO:0007829|PDB:1N7Z"
FT STRAND 294..297
FT /evidence="ECO:0007829|PDB:1N7Z"
FT HELIX 299..301
FT /evidence="ECO:0007829|PDB:1N7Z"
FT STRAND 307..318
FT /evidence="ECO:0007829|PDB:1N7Z"
FT STRAND 325..328
FT /evidence="ECO:0007829|PDB:1N7Z"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:1N7Z"
SQ SEQUENCE 334 AA; 38008 MW; 4997860773E14899 CRC64;
MNDSSVIYRA IVTSKFRTEK MLNFYNSIGS GPDKNTIFIT FGRSEPWSSN ENEVGFAPPY
PTDSVLGVTD MWTHMMGTVK VLPSMLDAVI PRRDWGDTRY PDPYTFRIND IVVCNSAPYN
ATESGAGWLV YRCLDVPDTG MCSIASLTDK DECLKLGGKW TPSARSMTPP EGRGDAEGTI
EPGDGYVWEY LFEIPPDVSI NRCTNEYIVV PWPEELKEDP TRWGYEDNLT WQQDDFGLIY
RVKANTIRFK AYLDSVYFPE AALPGNKGFR QISIITNPLE AKAHPNDPNV KAEKDYYDPE
DLMRHSGEMI YMENRPPIIM AMDQTEEINI LFTF
